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CATH Superfamily 3.40.50.720

NAD(P)-binding Rossmann-like Domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
NAD(P)-binding Rossmann-like Domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 68: Sorbitol dehydrogenase

There are 7 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
L-arabinitol 4-dehydrogenase. [EC: 1.1.1.12]
L-arabinitol + NAD(+) = L-xylulose + NADH.
    		 199 A0A024S5M7 A0A024S5M7 A0A024S5M7 A0A0B0EGC7 A0A0B0EGC7 A0A0B0EGC7 A0A0B0EGC7 A0A167UZD7 A0A167UZD7 A0A1L9N769
    (189 more...)
    D-xylulose reductase. [EC: 1.1.1.9]
    Xylitol + NAD(+) = D-xylulose + NADH.
    • Also acts as an L-erythrulose reductase.
    		 56 A0A178UB81 A0A178UB81 A0A1S9DIL5 A0A1S9DIL5 A0A1S9DIL5 A0A1S9DIL5 A0A364LYV1 A0A364LYV1 A0A364LYV1 A0A364LYV1
    (46 more...)
    L-iditol 2-dehydrogenase. [EC: 1.1.1.14]
    L-iditol + NAD(+) = L-sorbose + NADH.
    • This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals.
    • It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol.
    • Enzymes from different organisms or tissues display different substrate specificity.
    • The enzyme is specific to NAD(+) and can not use NADP(+).
    		 15 F6XVN0 F6XVN0 F6XVN0 G7PB87 G7PB87 G7PB87 P07846 P27867 Q00796 Q4R639
    (5 more...)
    L-threonine 3-dehydrogenase. [EC: 1.1.1.103]
    L-threonine + NAD(+) = L-2-amino-3-oxobutanoate + NADH.
    • Acts in concert with EC 2.3.1.29 in the degradation of threonine to glycine.
    • This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex.
    • In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone.
    		 8 B6YTJ5 I6UPN6 I6UPN6 O58389 Q5JI69 Q8U259 Q8U259 Q9UYX0
    Ribitol 2-dehydrogenase. [EC: 1.1.1.56]
    Ribitol + NAD(+) = D-ribulose + NADH.
      		 5 A0A178UB81 A0A178UB81 Q00796 Q9FJ95 Q9FJ95
      (R,R)-butanediol dehydrogenase. [EC: 1.1.1.4]
      (R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + NADH.
      • Also converts diacetyl into acetoin with NADH as reductant.
      		 5 N1P924 N1P924 P39714 P39714 Q00796
      Diacetyl reductase ((R)-acetoin forming). [EC: 1.1.1.303]
      (R)-acetoin + NAD(+) = diacetyl + NADH.
      • The reaction is catalyzed in the reverse direction.
      • This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76).
      • While the butanediol dehydrogenase activity is reversible, diacetyl reductase activity is irreversible.
      • This enzyme has been reported in the yeast Saccharomyces cerevisiae.
      • Different from EC 1.1.1.304.
      • Formerly EC 1.1.1.5.
      		 1 P39713
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